Reconstitution of a Heat Shock Effect in Vitro: Influence of GroE on the Thermal Aggregation of α-Glucosidase from Yeast

Bärbel Höll-Neugebauer, Rainer Rudolph, Marion Schmidt, Johannes Buchner

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109 Scopus citations

Abstract

α-Glucosidase from yeast is inactivated rapidly at temperatures above 42 °C. The thermal inactivation is accompanied by aggregation. The molecular chaperone GroEL suppresses the formation of aggregates by binding the thermally inactivated α-glucosidase. Spectroscopic studies suggest that GroEL binds α-glucosidase in an intermediately folded state. The complex between α-glucosidase and GroEL can be dissolved by MgATP. GroES accelerates the MgATP-dependent dissociation of the α-glucosidase-GroEL complex. At elevated temperatures this release leads to the formation of aggregates, while at lower temperatures native, enzymatically active molecules are formed.

Original languageEnglish
Pages (from-to)11609-11614
Number of pages6
JournalBiochemistry
Volume30
Issue number50
DOIs
StatePublished - 1 Dec 1991
Externally publishedYes

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